A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897837" target="_blank" >RIV/60076658:12310/18:43897837 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/18:00491852 RIV/00216224:14110/18:00105889 RIV/00159816:_____/18:00070384

Result on the web

<a href="https://link.springer.com/content/pdf/10.1007%2Fs00894-018-3722-8.pdf" target="_blank" >https://link.springer.com/content/pdf/10.1007%2Fs00894-018-3722-8.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-018-3722-8" target="_blank" >10.1007/s00894-018-3722-8</a>

Result language

angličtina

Original language name

A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I

Original language description

Type I restriction-modification enzymes differ significantly from the type II enzymes commonly used as molecular biology reagents. On hemi-methylated DNAs type I enzymes like the EcoR124I restriction-modification complex act as conventional adenine methylases at their specific target sequences, but unmethylated targets induce them to translocate thousands of base pairs through the stationary enzyme before cleaving distant sites nonspecifically. EcoR124I is a superfamily 2 DEAD-box helicase like eukaryotic double-strand DNA translocase Rad54, with two RecA-like helicase domains and seven characteristic sequence motifs that are implicated in translocation. In Rad54 a so-called extended region adjacent to motif III is involved in ATPase activity. Although the EcoR124I extended region bears sequence and structural similarities with Rad54, it does not influence ATPase or restriction activity as shown in this work, but mutagenesis of the conserved glycine residue of its motif III does alter ATPase and DNA cleavage activity. Through the lens of molecular dynamics, a full model of HsdR of EcoR124I based on available crystal structures allowed interpretation of functional effects of mutants in motif III and its extended region. The results indicate that the conserved glycine residue of motif III has a role in positioning the two helicase domains.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Volume of the periodical

24

Issue of the periodical within the volume

7

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

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UT code for WoS article

000436486600002

EID of the result in the Scopus database

2-s2.0-85049308208